YHFP_BACSU
ID YHFP_BACSU Reviewed; 330 AA.
AC O07615; Q796T7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative quinone oxidoreductase YhfP;
DE EC=1.6.5.-;
GN Name=yhfP; OrderedLocusNames=BSU10320;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Noback M.A., Terpstra P., Holsappel S., Venema G., Bron S.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "The structural study of hypothetical protein yhfP.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- SUBUNIT: Homodimer, or homotetramer. {ECO:0000305|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; Y14084; CAA74539.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12872.1; -; Genomic_DNA.
DR PIR; E69831; E69831.
DR RefSeq; NP_388913.1; NC_000964.3.
DR RefSeq; WP_003233163.1; NZ_JNCM01000035.1.
DR PDB; 1TT7; X-ray; 2.70 A; A/B/C/D/E/F=1-330.
DR PDB; 1Y9E; X-ray; 2.80 A; A/B/C/D/E/F=1-330.
DR PDBsum; 1TT7; -.
DR PDBsum; 1Y9E; -.
DR AlphaFoldDB; O07615; -.
DR SMR; O07615; -.
DR STRING; 224308.BSU10320; -.
DR PaxDb; O07615; -.
DR PRIDE; O07615; -.
DR DNASU; 939312; -.
DR EnsemblBacteria; CAB12872; CAB12872; BSU_10320.
DR GeneID; 939312; -.
DR KEGG; bsu:BSU10320; -.
DR PATRIC; fig|224308.179.peg.1109; -.
DR eggNOG; COG0604; Bacteria.
DR InParanoid; O07615; -.
DR OMA; RRFPCVG; -.
DR PhylomeDB; O07615; -.
DR BioCyc; BSUB:BSU10320-MON; -.
DR EvolutionaryTrace; O07615; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043957; F:acryloyl-CoA reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR InterPro; IPR014188; Acrylyl-CoA_reductase_AcuI.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43677:SF1; PTHR43677:SF1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02823; oxido_YhdH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..330
FT /note="Putative quinone oxidoreductase YhfP"
FT /id="PRO_0000360861"
FT BINDING 45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 160..163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 182..184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1TT7"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 122..144
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:1TT7"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:1TT7"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1Y9E"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:1TT7"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:1TT7"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:1TT7"
SQ SEQUENCE 330 AA; 34756 MW; 4B864054355D055C CRC64;
MSTLFQALQA EKNADDVSVH VKTISTEDLP KDGVLIKVAY SGINYKDGLA GKAGGNIVRE
YPLILGIDAA GTVVSSNDPR FAEGDEVIAT SYELGVSRDG GLSEYASVPG DWLVPLPQNL
SLKEAMVYGT AGFTAALSVH RLEQNGLSPE KGSVLVTGAT GGVGGIAVSM LNKRGYDVVA
STGNREAADY LKQLGASEVI SREDVYDGTL KALSKQQWQG AVDPVGGKQL ASLLSKIQYG
GSVAVSGLTG GGEVPATVYP FILRGVSLLG IDSVYCPMDV RAAVWERMSS DLKPDQLLTI
VDREVSLEET PGALKDILQN RIQGRVIVKL
